2B8A

High Resolution Structure of the HDGF PWWP Domain

2B8A の概要

• エントリーDOI: 10.2210/pdb2b8a/pdb
• 分子名称: Hepatoma-derived growth factor (1 entity in total)
• 機能のキーワード: pwwp, hdgf, hormone-growth factor complex, hormone/growth factor
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Cytoplasm (By similarity): Q8VHK7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12643.30

構造登録者

Lukasik, S.M.,Cierpicki, T.,Borloz, M.,Grembecka, J.,Everett, A.,Bushweller, J.H. (登録日: 2005-10-06, 公開日: 2005-12-06, 最終更新日: 2024-05-22)

主引用文献

Lukasik, S.M.,Cierpicki, T.,Borloz, M.,Grembecka, J.,Everett, A.,Bushweller, J.H.
High resolution structure of the HDGF PWWP domain: a potential DNA binding domain.
Protein Sci., 15:314-323, 2006

PubMed Abstract: Hepatoma Derived Growth Factor (HDGF) is an endogenous nuclear-targeted mitogen that is linked with human disease. HDGF is a member of the weakly conserved PWWP domain family. This 70-amino acid motif, originally identified from the WHSC1 gene, has been found in more than 60 eukaryotic proteins. In addition to the PWWP domain, many proteins in this class contain known chromatin remodeling domains, suggesting a role for HDGF in chromatin remodeling. We have determined the NMR structure of the HDGF PWWP domain to high resolution using a combination of NOEs, J-couplings, and dipolar couplings. Comparison of this structure to a previously determined structure of the HDGF PWWP domain shows a significant difference in the C-terminal region. Comparison to structures of other PWWP domains shows a high degree of similarity to the PWWP domain structures from Dnmt3b and mHRP. The results of selected and amplified binding assay and NMR titrations with DNA suggest that the HDGF PWWP domain may function as a nonspecific DNA-binding domain. Based on the NMR titrations, we propose a model of the interaction of the PWWP domain with DNA.

PubMed: 16384999
DOI: 10.1110/ps.051751706

実験手法

SOLUTION NMR